1k99
From Proteopedia
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Solution Structure of the first HMG box in human Upstream binding factor
Overview
Human upstream binding factor is a nucleolar transcription factor involved, in transcription by RNA polymerase I. It contains six HMG box domains; the, HMG box is a minor groove DNA-binding domain that has been found in, hundreds of proteins with different functions. Among the six HMG box, domains in hUBF, the first one can bind to the ribosomal promoter, specifically by itself and is essential for the whole protein's DNA, binding specificity. Here we report the three-dimensional structure of, this first HMG box free in solution determined by multidimensional NMR, using (13)C,(15)N-labeled protein. Like the previously determined HMG box, structures, hUBF HMG box 1 adopts a twisted L-shape consisting of three, alpha-helices: helix 1 (17-30) and helix 2 (38-51) pack onto each other to, form the short arm, while helix 3 (57-76) is associated with an extended, strand N-terminal to helix 1 and forms the long arm. A cluster of, conserved residues, in particular the aromatic residues F21, Y49, and Y60, is important to maintain the fold. The short arm is rigid due to extensive, hydrophobic interaction between helix 1 and helix 2, while the long arm is, less rigid.
About this Structure
1K99 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of the first HMG box domain in human upstream binding factor., Xu Y, Yang W, Wu J, Shi Y, Biochemistry. 2002 Apr 30;41(17):5415-20. PMID:11969401
Page seeded by OCA on Mon Nov 12 17:48:42 2007
Categories: Homo sapiens | Single protein | Shi, Y. | Wu, J. | Xu, Y. | Yang, W. | Alpha-helix | L-shape
